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  • Capillary water  (1)
  • Keywords: Alteromonas organophosphorus acid anhydrolase gene; X-Pro dipeptidase; sequencing and functional homology to prolidase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    The analysis of water in the Martian regolith (1979)
    Springer
    Journal of molecular evolution 14 (1979), S. 33-38 
    Details
    ISSN: 1432-1432
    Keywords: Water ; Mars ; Adsorbed water ; Capillary water ; Mineral hydrates-hygroscopic minerals ; Endolithic organisms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary One of the scientific objectives of the Viking Mission to Mars was to accomplish an analysis of water in the Martian regolith. The analytical scheme originally envisioned was severly compromised in the latter stages of the Lander instrument package design. Nevertheless, a crude soil water analysis was accomplished. Samples from each of the two widely separated sites yielded roughly 1 to 3% water by weight when heated successively to several temperatures up to 500°C. A significant portion of this water was released in the 200° to 350°C interval indicating the presence of mineral hydrates of relatively low thermal stability, a finding in keeping with the low temperatures generally prevailing on Mars. The presence of a duricrust at one of the Lander sites is taken as possible evidence for the presence of hygroscopic minerals on Mars. The demonstrated presence of atmospheric water vapor and thermodynamic calculations lead to the belief that adsorbed water could provide a relatively favorable environment for endolithic organisms on Mars similar to types recently discovered in the dry antarctic deserts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01732365
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  • 2
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis (1997)
    Springer
    Journal of industrial microbiology and biotechnology 18 (1997), S. 49-55 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: Alteromonas organophosphorus acid anhydrolase gene; X-Pro dipeptidase; sequencing and functional homology to prolidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Organophosphorus acid anhydrolases (OPAA) catalyzing the hydrolysis of a variety of toxic organophosphorus cholinesterase inhibitors offer potential for decontamination of G-type nerve agents and pesticides. The gene (opa) encoding an OPAA was cloned from the chromosomal DNA of Alteromonas haloplanktis ATCC 23821. The nucleotide sequence of the 1.7-kb DNA fragment contained the opa gene (1.3 kb) and its flanking region. We report structural and functional similarity of OPAAs from A. haloplanktis and Alteromonas sp JD6.5 with the enzyme prolidase that hydrolyzes dipeptides with a prolyl residue in the carboxyl-terminal position. These results corroborate the earlier conclusion that the OPAA is a type of X-Pro dipeptidase, and that X-Pro could be the native substrate for such an enzyme in Alteromonas cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900358
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    Paper (German National Licenses)
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